Abstract
The metallo-β-lactamases (MβLs) constitute a very ancient family of enzymes with a wide range of substrates, including RNA and DNA. The β-lactamases that act on RNA (here called rMβLs) can be grouped into two major families, the RNase Z family and the β-CASP family. Members of the RNase Z family are primarily involved in the maturation of the 3′ end of tRNAs, whereas members of the β-CASP family have thus far been shown to have primarily mRNA and snRNA targets. Although they share a metallo-β-lactamase core and catalytic mechanism, the two families are easily distinguishable at the sequence level and by the presence of characteristic subdomains that play a key role in substrate recognition. These are principally the so-called flexible arm (about 40 amino-acids) of RNase Z and the β-CASP domain (>160 amino-acids) that gives its name to this family of enzymes. In this chapter, I will describe our current understanding of these two MβL families, with particular emphasis on their structures, their substrates, and their phylogenic distribution.
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Acknowledgments
This work was supported by funds from the CNRS (UPR 9073), Université Paris VII-Denis Diderot and the Agence Nationale de la Recherche (ANR- SubtilRNA2). I thank colleagues and current and former lab members for their contributions to the data discussed in this chapter. I also thank Béatrice Clouet-d’Orval, Zbigniew Dominski, and Allen Nicholson for their helpful comments on the manuscript.
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Condon, C., Gilet, L. (2011). The Metallo-β-Lactamase Family of Ribonucleases. In: Nicholson, A. (eds) Ribonucleases. Nucleic Acids and Molecular Biology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-21078-5_10
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